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2007-07-05Zeitschriftenartikel DOI: 10.1186/1471-2180-7-67
The Yersinia enterocolitica type three secretion chaperone SycO is integrated into the Yop regulatory network and binds to the Yop secretion protein YscM1
dc.contributor.authorDittmann, Svea
dc.contributor.authorSchmid, Annika
dc.contributor.authorRichter, Susanna
dc.contributor.authorTrülzsch, Konrad
dc.contributor.authorHeesemann, Jürgen
dc.contributor.authorWilharm, Gottfried
dc.date.accessioned2018-05-07T13:47:22Z
dc.date.available2018-05-07T13:47:22Z
dc.date.created2010-03-23
dc.date.issued2007-07-05none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/recHzITf1lpmc/PDF/24rr3jSfIq.pdf
dc.identifier.urihttp://edoc.rki.de/176904/611
dc.description.abstractBackground: Pathogenic yersiniae (Y. pestis, Y. pseudotuberculosis, Y. enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS). This T3SS comprises more than 40 constituents. Among these are the transport substrates called Yops (Yersinia outer proteins), the specific Yop chaperones (Sycs), and the Ysc (Yop secretion) proteins which form the transport machinery. The effectors YopO and YopP are encoded on an operon together with SycO, the chaperone of YopO. The characterization of SycO is the focus of this study. Results: We have established the large-scale production of recombinant SycO in its outright form. We confirm that Y. enterocolitica SycO forms homodimers which is typical for Syc chaperones. SycO overproduction in Y. enterocolitica decreases secretion of Yops into the culture supernatant suggesting a regulatory role of SycO in type III secretion. We demonstrate that in vitro SycO interacts with YscM1, a negative regulator of Yop expression in Y. enterocolitica. However, the SycO overproduction phenotype was not mediated by YscM1, YscM2, YopO or YopP as revealed by analysis of isogenic deletion mutants. Conclusion: We present evidence that SycO is integrated into the regulatory network of the Yersinia T3SS. Our picture of the Yersinia T3SS interactome is supplemented by identification of the SycO/YscM1 interaction. Further, our results suggest that at least one additional interaction partner of SycO has to be identified.ger
dc.language.isoeng
dc.publisherRobert Koch-Institut
dc.subjectBacterialeng
dc.subjectGene Expression Regulationeng
dc.subjectProtein Bindingeng
dc.subjectTranscription Factors/metabolismeng
dc.subjectBacterial Proteins/metabolismeng
dc.subjectDimerizationeng
dc.subjectMolecular Chaperones/metabolismeng
dc.subjectProtein Transport/geneticseng
dc.subjectProtein Transport/physiologyeng
dc.subjectYersinia enterocolitica/geneticseng
dc.subjectYersinia enterocolitica/metabolismeng
dc.subjectYersinia enterocolitica/physiologyeng
dc.subject.ddc610 Medizin
dc.titleThe Yersinia enterocolitica type three secretion chaperone SycO is integrated into the Yop regulatory network and binds to the Yop secretion protein YscM1
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-1006218
dc.identifier.doi10.1186/1471-2180-7-67
dc.identifier.doihttp://dx.doi.org/10.25646/536
local.edoc.container-titleBMC Microbiology
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://www.biomedcentral.com/1471-2180/7/67
local.edoc.container-publisher-nameBioMedCentral
local.edoc.container-volume7
local.edoc.container-issue67
local.edoc.container-year2007

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